Reviewed, UniProtKB/Swiss-Prot P28173 (PUR1_CHICK)

Names and origin

Protein names

Recommended name:
    Amidophosphoribosyltransferase
      Short name=ATase
    EC=2.4.2.14
Alternative name(s):
    Glutamine phosphoribosylpyrophosphate amidotransferase
      Short name=GPAT

Gene names

Name:	PPAT
Synonyms:	GPAT

Organism

Gallus gallus (Chicken)

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	510 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O.
Cofactor	Binds 1 magnesium ion per subunit By similarity. Binds 1 4Fe-4S cluster per subunit By similarity.
Pathway	Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2.
Subunit structure	Homotetramer.
Sequence similarities	In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family. Contains 1 glutamine amidotransferase type-2 domain.

Ontologies

Keywords
Biological process	Purine biosynthesis
Domain	Glutamine amidotransferase
Ligand	4Fe-4S Iron Iron-sulfur Magnesium Metal-binding
Molecular function	Glycosyltransferase Transferase
Technical term	Allosteric enzyme
Gene Ontology (GO)
Biological process	glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW nucleoside metabolic process Inferred from electronic annotation. Source: InterPro purine base biosynthetic process Inferred from electronic annotation. Source: InterPro purine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW amidophosphoribosyltransferase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 11	11	Probable		PRO_0000029281
	Chain	12 – 510	499	Amidophosphoribosyltransferase		PRO_0000029282
Regions
	Domain	12 – 261	250	Glutamine amidotransferase type-2
Sites
	Active site	12	1	For GATase activity By similarity
	Metal binding	280	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	327	1	Magnesium By similarity
	Metal binding	389	1	Magnesium By similarity
	Metal binding	390	1	Magnesium By similarity
	Metal binding	426	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	496	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	499	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P28173-1 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: F4371FE1FEC7C744	FASTA	510	56,257
	10 20 30 40 50 60 MELEELGIRE ECGVFGCIAA GVWPTELDVP HVITLGLVGL QHRGQESAGI VTSDGESSQA 70 80 90 100 110 120 FKVHKGMGLI NHVFNADSLK KLYVSNLGIG HTRYSTSGIS ELQNCQPFVV ETLHGKIAVA 130 140 150 160 170 180 HNGELTNAVR LRRKLMRHGV GLSTSSDSEL ITQLLAFTPP LENDDTADWV ARIKNLMNET 190 200 210 220 230 240 PTSYSLLIMH KDIIYAVRDP YGNRPLCIGR LIPVGDINGK GKDNSETEGW VVSSESCSFL 250 260 270 280 290 300 SIGAEYYREV LPGEIVKISR YDVQTLDVVP RPEGDPSAFC IFEYVYFARP DSIFEGQMVY 310 320 330 340 350 360 SVRRRCGQQL AIEAPVEADL VSTVPESATP AALGYAQKCG LPYVEVLCKN RYVGRTFIQP 370 380 390 400 410 420 NMRLRQLGVA KKFGVLSDNF KGKRVVIIDD SIVRGNTISP IIKLLRESGA KEVHIRVASP 430 440 450 460 470 480 PIRFPCYMGI NIPTKEELIA NRPEFHDLAN YIGADSVVYL SVEGLVSSVQ ESIKARKENE 490 500 510 NSLKTQKSRV GKIGHCTACL TGDYPVELEW

References

[1]	"Cloning and expression of avian glutamine phosphoribosylpyrophosphate amidotransferase. Conservation of a bacterial propeptide sequence supports a role for posttranslational processing." Zhou G., Dixon J.E., Zalkin H. J. Biol. Chem. 265:21152-21159(1990) [PubMed: 2123487] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Coexpression of two closely linked avian genes for purine nucleotide synthesis from a bidirectional promoter." Gavalas A., Dixon J.E., Brayton K.A., Zalkin H. Mol. Cell. Biol. 13:4784-4792(1993) [PubMed: 8336716] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1-42.
[3]	Erratum Gavalas A., Dixon J.E., Brayton K.A., Zalkin H. Mol. Cell. Biol. 13:7977-7977(1993)

Cross-references

Sequence databases
EMBLGenBankDDBJ	M60069 mRNA. Translation: AAA62736.1. L12533 Unassigned DNA. Translation: AAA17895.1.
IPI	IPI00581378.
PIR	A38337.
RefSeq	NP_001004401.1.
UniGene	Gga.2870
3D structure databases
HSSP	HSSP built from PDB template 1AO0 based on UniProtKB P00497.
ModBase	Search...
Protein-protein interaction databases
STRING	P28173.
Protein family/group databases
MEROPS	C44.001.
Genome annotation databases
Ensembl	ENSGALT00000022312; ENSGALP00000022273; ENSGALG00000013728; Gallus gallus. [Genome view]
GeneID	422743.
KEGG	gga:422743.
Organism-specific databases
CTD	422743.
Phylogenomic databases
HOGENOM	P28173.
HOVERGEN	P28173.
Enzyme and pathway databases
BRENDA	2.4.2.14. 4.
Family and domain databases
InterPro	IPR005854. Amd_phspho_trans. IPR000583. GATase_2. IPR017932. GATase_II. IPR002375. Pr/py_Pribosyl_transf_CS. IPR000836. PRibTrfase. [Graphical view]
PANTHER	PTHR11907. Amd_phspho_trans. 1 hit.
Pfam	PF00310. GATase_2. 1 hit. PF00156. Pribosyltran. 1 hit. [Graphical view]
PIRSF	PIRSF000485. Amd_phspho_trans. 1 hit.
TIGRFAMs	TIGR01134. purF. 1 hit.
PROSITE	PS51278. GATASE_TYPE_2. 1 hit. PS00103. PUR_PYR_PR_TRANSFER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PUR1_CHICK

Accession

Primary (citable) accession number: P28173

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	September 1, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)